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http://hdl.handle.net/2445/135597
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DC Field | Value | Language |
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dc.contributor.author | Nicot, Carine | - |
dc.contributor.author | Relat Pardo, Joana | - |
dc.contributor.author | Woldegiorgis, Gebre | - |
dc.contributor.author | Haro Bautista, Diego | - |
dc.contributor.author | Marrero González, Pedro F. | - |
dc.date.accessioned | 2019-06-20T09:15:45Z | - |
dc.date.available | 2019-06-20T09:15:45Z | - |
dc.date.issued | 2002-03 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/2445/135597 | - |
dc.description.abstract | Pig and rat liver carnitine palmitoyltransferase I (L-CPTI) share common K(m) values for palmitoyl-CoA and carnitine. However, they differ widely in their sensitivity to malonyl-CoA inhibition. Thus, pig l-CPTI has an IC(50) for malonyl-CoA of 141 nm, while that of rat L-CPTI is 2 microm. Using chimeras between rat L-CPTI and pig L-CPTI, we show that the entire C-terminal region behaves as a single domain, which dictates the overall malonyl-CoA sensitivity of this enzyme. The degree of malonyl-CoA sensitivity is determined by the structure adopted by this domain. Using deletion mutation analysis, we show that malonyl-CoA sensitivity also depends on the interaction of this single domain with the first 18 N-terminal amino acid residues. We conclude that pig and rat L-CPTI have different malonyl-CoA sensitivity, because the first 18 N-terminal amino acid residues interact differently with the C-terminal domain. This is the first study that describes how interactions between the C- and N-terminal regions can determine the malonyl-CoA sensitivity of L-CPTI enzymes using active C-terminal chimeras. | - |
dc.format.extent | 6 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1074/jbc.M109976200 | - |
dc.relation.ispartof | Journal of Biological Chemistry, 2002, vol. 277, num. 12, p. 10044-10049 | - |
dc.relation.uri | https://doi.org/10.1074/jbc.M109976200 | - |
dc.rights | (c) American Society for Biochemistry and Molecular Biology, 2002 | - |
dc.source | Articles publicats en revistes (Nutrició, Ciències de l'Alimentació i Gastronomia) | - |
dc.subject.classification | Carnitina palmitoïl-transferasa 1 | - |
dc.subject.classification | Cinètica enzimàtica | - |
dc.subject.classification | Aminoàcids | - |
dc.subject.classification | Mutagènesi | - |
dc.subject.other | Carnitine palmitoyltransferase I | - |
dc.subject.other | Enzyme kinetics | - |
dc.subject.other | Amino acids | - |
dc.subject.other | Mutagenesis | - |
dc.title | Pig liver carnitine palmitoyltransferase. Chimera studies show that both the N- and C-terminal regions of the enzyme are important for the unusual high malonyl-CoA sensitivity | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 527447 | - |
dc.date.updated | 2019-06-20T09:15:45Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 11790778 | - |
Appears in Collections: | Articles publicats en revistes (Nutrició, Ciències de l'Alimentació i Gastronomia) |
Files in This Item:
File | Description | Size | Format | |
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527447.pdf | 140.97 kB | Adobe PDF | View/Open |
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